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1qub

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(New page: 200px<br /> <applet load="1qub" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qub, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1qub.gif|left|200px]]<br />
 
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<applet load="1qub" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qub, resolution 2.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMA'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMA==
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Human beta(2)-glycoprotein I is a heavily glycosylated five-domain plasma, membrane-adhesion protein, which has been implicated in blood coagulation, and clearance of apoptotic bodies from the circulation. It is also the key, antigen in the autoimmune disease anti-phospholipid syndrome. The crystal, structure of beta(2)-glycoprotein I isolated from human plasma reveals an, elongated fish-hook-like arrangement of the globular short consensus, repeat domains. Half of the C-terminal fifth domain deviates strongly from, the standard fold, as observed in domains one to four. This aberrant half, forms a specific phospholipid-binding site. A large patch of 14 positively, charged residues provides electrostatic interactions with anionic, phospholipid headgroups and an exposed membrane-insertion loop yields, specificity for lipid layers. The observed spatial arrangement of the five, domains suggests a functional partitioning of protein adhesion and, membrane adhesion over the N- and C-terminal domains, respectively, separated by glycosylated bridging domains. Coordinates are in the Protein, Data Bank (accession No. 1QUB).
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<StructureSection load='1qub' size='340' side='right'caption='[[1qub]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1qub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUB FirstGlance]. <br>
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Known disease associated with this structure: Apolipoprotein H deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138700 138700]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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==About this Structure==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qub OCA], [https://pdbe.org/1qub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qub RCSB], [https://www.ebi.ac.uk/pdbsum/1qub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qub ProSAT]</span></td></tr>
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1QUB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QUB OCA].
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</table>
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== Function ==
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==Reference==
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[https://www.uniprot.org/uniprot/APOH_HUMAN APOH_HUMAN] Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
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Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure., Bouma B, de Groot PG, van den Elsen JM, Ravelli RB, Schouten A, Simmelink MJ, Derksen RH, Kroon J, Gros P, EMBO J. 1999 Oct 1;18(19):5166-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10508150 10508150]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/1qub_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qub ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bouma, B.]]
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[[Category: Bouma B]]
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[[Category: Derksen, R.H.W.M.]]
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[[Category: Derksen RHWM]]
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[[Category: Elsen, J.M.H.van.den.]]
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[[Category: Gros P]]
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[[Category: Groot, Ph.G.de.]]
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[[Category: Kroon J]]
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[[Category: Gros, P.]]
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[[Category: Ravelli RBG]]
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[[Category: Kroon, J.]]
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[[Category: Schouten A]]
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[[Category: Ravelli, R.B.G.]]
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[[Category: Simmelink MJA]]
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[[Category: Schouten, A.]]
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[[Category: De Groot PG]]
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[[Category: Simmelink, M.J.A.]]
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[[Category: Van den Elsen JMH]]
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[[Category: NAG]]
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[[Category: complement control protein]]
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[[Category: membrane adhesion]]
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[[Category: multi-domain]]
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[[Category: n-glycosylation]]
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[[Category: short consensus repeat]]
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[[Category: sushi]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:56:43 2007''
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Current revision

CRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMA

PDB ID 1qub

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